Effects of ablation of the pars intercerebralis on ecdysteroid quantities and yolk protein expression in the blowfly Protophormia terraenovae

Quantities of ecdysteroid are compared in the haemolymph and ovaries of the blowfly Protophormia terraenovae Robineau‐Desvoidy (Diptera: Calliphoridae) under reproductive (LD 18 : 6 h at 25 °C) and diapause (LD 12 : 12 h at 20 °C) conditions. The effects of ablation of the pars intercerebralis or ovaries on ecdysteroid quantities and of ablation of the pars intercerebralis on yolk protein expression are examined. Under reproductive conditions, the levels of ecdysteroid in vitellogenic females are high, although the levels in previtellogenic females and females with mature ovaries are low. Under diapause conditions, there are low quantities of ecdysteroid in both the haemolymph and ovaries. Ecdysteroid titres in the haemolymph are not significantly affected by the removal of the ovaries, suggesting that tissues other than the ovaries are also involved in the production of ecdysteroids. Reproductive females in which the pars intercerebralis of the brain is experimentally ablated have ecdysteroid levels that are not significantly different from sham‐operated or intact females. However, yolk protein expression in the fat body is suppressed after removal of the pars intercerebralis. These results suggest that the suppression of ecdysteroid levels in the haemolymph and ovaries is associated with reproductive diapause, and that the pars intercerebralis could play a role in yolk protein synthesis without mediating ecdysteroid production.     

NUCLEAR ANTIGENS,AS DNA,OF DSB389 MAB AND SOME OTHER ANTI-DESMIN MONOCLONAL ANTIBODIES

The anti-desmin monoclonal antibodies (MAbs) DSB389, AC54, and DSB860 recognize intermediate filaments (IFs) and nuclear antigens that appear granular, locate around chromosomes, and are insoluble following 0.5% Triton X-100 and cetyltrimethylammonium bromide (CTAB) extraction. Nuclear antigens of the MAbs were searched for in an IFs-deficient clone of SW13 cells. Reactive materials specific to DSB389, AC54, and DSB860 MAbs were trapped at the top of the gel of SDS—agarose—PAGE. The reactivity of the materials disappeared after treatment with DNase I. The reactivity, or trapping of this material at the top of the gel, required previous heat treatment of the sample before application to the gel. The MAbs recognized both single-stranded and double-stranded DNA in ELISA. These results indicate that at least the main nuclear antigens of DSB389, DSB860 and AC54 MAbs are DNA.     

STUDIES ON PROTEIN METABOLISM IN HIGHER PLANTS. III. CHANGES IN THE SOLUBLE PROTEIN COMPONENTS WITH LEAF GROWTH

Water soluble protein was extracted from tobacco leaves (BrightYellow) and fractionated through chromatographic and immunochemicalprocedures. Six different UV-absorbing components, 7 antigeniccomponents, and 4 enzyme activities (phosphatase, protease,peroxidase and RNase) were detected on the Sephadex chromatogramsof leaf extracts. An UV-absorbing fraction, Fr. I-2, (immunochemicallydesignated as Pr. Imm-I) corresponded to the known "FractionI " of S. G. WILDMAN. The contents of the three antigenic components,Imm-a, Imm-b and Imm-c, having estimated molecular weights of1 to 2 10⁵, showed significant fluctuations during growthof the leaves. Peroxidase and another antigenic component (Imm-f)of smaller molecular weight showed increase with age of theleaves. Properties of the protein components thus detected wereinvestigated. (Received May 11, 1967; )     

STUDIES ON PROTEIN METABOLISM IN HIGHER PLANTS IV. CHANGES IN PROTEIN COMPONENTS IN DETACHED LEAVES OF TOBACCO

Soluble protein fractions from tobacco leaves before and aftercuring were compared. The results of Sephadex G-200 or G-75chromatography and immunological experiments showed that theamount of larger molecular weight proteins diminished or greatlydecreased and that smaller molecular weight proteins accumulatedduring 3 days at 40 and 90% humidity after excision of theleaves from the stem. Fraction I, which was the largest proteinin the leaf extract and occupied about one-half of the solubleprotein before curing, was not found in the proteins after curing.On the contrary, the proteins contained in II-4 fraction, whichwere supposed to have smaller molecular weights, increased three-foldduring the curing. The origin of the smaller proteins was discussed. (Received May 11, 1967; )